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1gtl

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(New page: 200px<br /> <applet load="1gtl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gtl, resolution 2.8&Aring;" /> '''THE THERMOSTABLE SER...)
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==About this Structure==
==About this Structure==
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1GTL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_novosp._mn-32 Bacillus novosp. mn-32]] with CA, SO4 and ACE as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTL OCA]].
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1GTL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacteria Bacteria]] with CA, SO4 and ACE as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTL OCA]].
==Reference==
==Reference==
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12057200 12057200]
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12057200 12057200]
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[[Category: Bacillus novosp. mn-32]]
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[[Category: Bacteria]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bode, W.]]
[[Category: Bode, W.]]
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[[Category: thermostable]]
[[Category: thermostable]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:25:46 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:18:07 2007''

Revision as of 11:13, 30 October 2007


1gtl, resolution 2.8Å

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THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLYSIN- COMPLEX WITH AC-ILE-PRO-PHE-CHO

Overview

Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the, newly identified family of serine-carboxyl proteinases, which also, includes CLN2, a human lysosomal homolog recently implicated in a fatal, neurodegenerative disease. Kumamolysin and its complexes with two aldehyde, inhibitors were crystallized, and their three-dimensional structures were, solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas, homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with, particularly short interconnecting hydrogen bonds and an oxyanion hole, enabling the reactive serine to attack substrate peptide bonds at quite, acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might, ... [(full description)]

About this Structure

1GTL is a [Single protein] structure of sequence from [Bacteria] with CA, SO4 and ACE as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:12057200

Page seeded by OCA on Tue Oct 30 13:18:07 2007

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